7nac: Difference between revisions
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New page: '''Unreleased structure''' The entry 7nac is ON HOLD Authors: Cruz, V.E., Sekulski, K., Peddada, N., Erzberger, J.P. Description: State E2 nucleolar 60S ribosomal biogenesis intermedia... |
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==State E2 nucleolar 60S ribosomal biogenesis intermediate - Composite model== | |||
<StructureSection load='7nac' size='340' side='right'caption='[[7nac]], [[Resolution|resolution]] 3.04Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7nac]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_BY4741 Saccharomyces cerevisiae BY4741]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7NAC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7NAC FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.04Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A2M:2-O-METHYLADENOSINE+5-(DIHYDROGEN+PHOSPHATE)'>A2M</scene>, <scene name='pdbligand=OMG:O2-METHYLGUANOSINE-5-MONOPHOSPHATE'>OMG</scene>, <scene name='pdbligand=OMU:O2-METHYLURIDINE+5-MONOPHOSPHATE'>OMU</scene>, <scene name='pdbligand=PSU:PSEUDOURIDINE-5-MONOPHOSPHATE'>PSU</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7nac FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7nac OCA], [https://pdbe.org/7nac PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7nac RCSB], [https://www.ebi.ac.uk/pdbsum/7nac PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7nac ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/LOC1_YEAST LOC1_YEAST] Required for efficient assembly and nuclear export of the 60S ribosomal subunit. Involved in asymmetric localization of ASH1 mRNA.<ref>PMID:11309412</ref> <ref>PMID:16871394</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
DEAD-box ATPases are ubiquitous enzymes essential in all aspects of RNA biology. However, the limited in vitro catalytic activities described for these enzymes are at odds with their complex cellular roles, most notably in driving large-scale RNA remodeling steps during the assembly of ribonucleoproteins (RNPs). We describe cryo-EM structures of 60S ribosomal biogenesis intermediates that reveal how context-specific RNA unwinding by the DEAD-box ATPase Spb4 results in extensive, sequence-specific remodeling of rRNA secondary structure. Multiple cis and trans interactions stabilize Spb4 in a post-catalytic, high-energy intermediate that drives the organization of the three-way junction at the base of rRNA domain IV. This mechanism explains how limited strand separation by DEAD-box ATPases is leveraged to provide non-equilibrium directionality and ensure efficient and accurate RNP assembly. | |||
Sequence-specific remodeling of a topologically complex RNP substrate by Spb4.,Cruz VE, Sekulski K, Peddada N, Sailer C, Balasubramanian S, Weirich CS, Stengel F, Erzberger JP Nat Struct Mol Biol. 2022 Dec;29(12):1228-1238. doi: 10.1038/s41594-022-00874-9. , Epub 2022 Dec 8. PMID:36482249<ref>PMID:36482249</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Cruz | <div class="pdbe-citations 7nac" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: Peddada | ==See Also== | ||
[[Category: | *[[GTP-binding protein 3D structures|GTP-binding protein 3D structures]] | ||
*[[Ribosome 3D structures|Ribosome 3D structures]] | |||
*[[Ribosome biogenesis protein 3D structures|Ribosome biogenesis protein 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Saccharomyces cerevisiae BY4741]] | |||
[[Category: Cruz VE]] | |||
[[Category: Erzberger JP]] | |||
[[Category: Peddada N]] | |||
[[Category: Sekulski K]] | |||
Latest revision as of 08:45, 5 June 2024
State E2 nucleolar 60S ribosomal biogenesis intermediate - Composite modelState E2 nucleolar 60S ribosomal biogenesis intermediate - Composite model
Structural highlights
FunctionLOC1_YEAST Required for efficient assembly and nuclear export of the 60S ribosomal subunit. Involved in asymmetric localization of ASH1 mRNA.[1] [2] Publication Abstract from PubMedDEAD-box ATPases are ubiquitous enzymes essential in all aspects of RNA biology. However, the limited in vitro catalytic activities described for these enzymes are at odds with their complex cellular roles, most notably in driving large-scale RNA remodeling steps during the assembly of ribonucleoproteins (RNPs). We describe cryo-EM structures of 60S ribosomal biogenesis intermediates that reveal how context-specific RNA unwinding by the DEAD-box ATPase Spb4 results in extensive, sequence-specific remodeling of rRNA secondary structure. Multiple cis and trans interactions stabilize Spb4 in a post-catalytic, high-energy intermediate that drives the organization of the three-way junction at the base of rRNA domain IV. This mechanism explains how limited strand separation by DEAD-box ATPases is leveraged to provide non-equilibrium directionality and ensure efficient and accurate RNP assembly. Sequence-specific remodeling of a topologically complex RNP substrate by Spb4.,Cruz VE, Sekulski K, Peddada N, Sailer C, Balasubramanian S, Weirich CS, Stengel F, Erzberger JP Nat Struct Mol Biol. 2022 Dec;29(12):1228-1238. doi: 10.1038/s41594-022-00874-9. , Epub 2022 Dec 8. PMID:36482249[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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